Evidence map›Paper›PMID 10768933›Full record

ArticleInfection and immunity2000

pH-induced conformational changes in Clostridium difficile toxin B.

M Qa'Dan, L M Spyres, J D Ballard

Abstract read
In one paragraph

Article in Infection and immunity, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
2.5field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

81 citing papers in PubMed, 152 citations in OpenAlex.

  1. Article
  2. AgainstToxins · 2025
    Review
  3. Allosterically switchable network orientsProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Mechanisms ofFrontiers in cellular and infection microbiology · 2025
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Structure and conformational dynamics ofLife science alliance · 2022
    Article
  14. Article
  15. Human α-Defensin-6 NeutralizesInternational journal of molecular sciences · 2022
    Article
  16. Article
  17. Article
  18. Neutralizing epitopes onFrontiers in immunology · 2022
    Article
  19. Article
  20. Large Clostridial Toxins: Mechanisms and Roles in Disease.Microbiology and molecular biology reviews : MMBR · 2021
    Review

21 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

M Qa'DanDepartment of Botany and Microbiology, The University of Oklahoma, Norman, Oklahoma 73019, USA.
L M Spyres
J D Ballard
University of Oklahoma · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Toxin B from Clostridium difficile is a monoglucosylating toxin that targets substrates within the cytosol of mammalian cells. In this study, we investigated the impact of acidic pH on cytosolic entry and structural changes within toxin B. Bafilomycin A1 was used to block endosomal acidification and subsequent toxin B translocation. Cytopathic effects could be completely blocked by addition of bafilomycin A1 up to 20 min following toxin treatment. Furthermore, providing a low extracellular pH could circumvent the effect of bafilomycin A1 and other lysosomotropic agents. Acid pH-induced structural changes were monitored by using the fluorescent probe 2-(p-toluidinyl) naphthalene-6-sulfonic acid, sodium salt (TNS), inherent tryptophan fluorescence, and relative susceptibility to a specific protease. As the toxin was exposed to lower pH there was an increase in TNS fluorescence, suggesting the exposure of hydrophobic domains by toxin B. The change in hydrophobicity appeared to be reversible, since returning the pH to neutrality abrogated TNS fluorescence. Furthermore, tryptophan fluorescence was quenched at the acidic pH, indicating that domains may have been moving into more aqueous environments. Toxin B also demonstrated variable susceptibility to Staphylococcus aureus V8 protease at neutral and acidic pH, further suggesting pH-induced structural changes in this protein.

Indexed as

Bacterial ProteinsMacrolidesProtein ConformationAnimalsAnti-Bacterial AgentsBacterial ToxinsCHO CellsClostridioides difficileCricetinaeCytotoxinsEnzyme InhibitorsFluorescent DyesHydrogen-Ion ConcentrationNaphthalenesulfonatesProton-Translocating ATPasesSerine EndopeptidasesAnti-Bacterial AgentsBacterial ProteinsBacterial Toxinsbafilomycin A1CytotoxinsEnzyme InhibitorsFluorescent Dyesglutamyl endopeptidaseMacrolidesNaphthalenesulfonatesProton-Translocating ATPasesSerine EndopeptidasestoxB protein, Clostridium difficileTryptophan

Identifiers

PMID10768933
PMCPMC97448
OpenAlexW2115878336

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.